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  • Discovery of the first potent and selective Mycobacterium tuberculosis Zmp1 inhibitor.

    Bioorg Med Chem Lett. 24(11):2508-11. doi: 10.1016/j.bmcl.2014.04.004. June 1, 2014. View on PubMed.
  • Authors

    Mori M, Moraca F, Deodato D, Ferraris DM, Selchow P, Sander P, Rizzi M, and Botta M
  • Abstract

    The Mycobacterium tuberculosis extracellular zinc metalloprotease 1 (Zmp1) has been proposed to play a key role in phagosome maturation and to enhance the survival of Mycobacterium tuberculosis in the host. Consequently, small molecule inhibitors of Zmp1 are of pivotal importance as a tool to better understand the pathogenicity of Zmp1 and as lead candidates for pharmacological intervention. Here we combined in silico structure-based inhibitor design with biochemical studies to discover and characterize the first potent competitive Zmp1 inhibitor showing a Ki of 94 nM and a high selectivity for Zmp1 with respect to human Neprilysin.

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